AMINO ACIDS SEQUENCE ANALYSIS ON COLLAGEN
Abstract
Staring from available information about amino acids properties and sequences on collagen type I chains. the aims of the study were to identify the principal property component and to analyze the similarities within and between collagens on five species. The principal component analysis applied on twenty-four amino acids properties revealed that the hydrophobic or hydrophilic character measured by Wealling et al. is more stable comparing with the other investigated properties. Similarity analysis identified similar and dissimilar within and between studied species from the viewpoint of amino acids sequences on collagen type I alpha 1 and 2 chains.a) Authors retain copyright and grant the journal right of first publication with the work simultaneously licensed under a Creative Commons Attribution License that allows others to share the work with an acknowledgement of the work's authorship and initial publication in this journal.
b) Authors are able to enter into separate, additional contractual arrangements for the non-exclusive distribution of the journal's published version of the work (e.g., post it to an institutional repository or publish it in a book), with an acknowledgement of its initial publication in this journal.
c) Authors are permitted and encouraged to post their work online (e.g., in institutional repositories or on their website) prior to and during the submission process, as it can lead to productive exchanges, as well as earlier and greater citation of published work (See The Effect of Open Access).